| Year |
Citation |
Score |
| 2022 |
Avagyan S, Makhatadze GI. Volumetric Properties of the Transition State Ensemble for Protein Folding. The Journal of Physical Chemistry. B. 126: 7615-7620. PMID 36150186 DOI: 10.1021/acs.jpcb.2c05437 |
0.301 |
|
| 2022 |
Pulavarti SVSRK, Maguire JB, Yuen S, Harrison JS, Griffin J, Premkumar L, Esposito EA, Makhatadze GI, Garcia AE, Weiss TM, Snell EH, Kuhlman B, Szyperski T. From Protein Design to the Energy Landscape of a Cold Unfolding Protein. The Journal of Physical Chemistry. B. PMID 35128921 DOI: 10.1021/acs.jpcb.1c10750 |
0.364 |
|
| 2020 |
Xu SCS, LoRicco JG, Bishop AC, James NA, Huynh WH, McCallum SA, Roan NR, Makhatadze GI. Sequence-independent recognition of the amyloid structural motif by GFP protein family. Proceedings of the National Academy of Sciences of the United States of America. PMID 32839332 DOI: 10.1073/Pnas.2001457117 |
0.359 |
|
| 2019 |
Avagyan S, Vasilchuk D, Makhatadze GI. Protein Adaptation to High Hydrostatic Pressure: Computational Analysis of the Structural Proteome. Proteins. PMID 31618488 DOI: 10.1002/Prot.25839 |
0.383 |
|
| 2018 |
Matsuura Y, Takehira M, Makhatadze GI, Joti Y, Naitow H, Kunishima N, Yutani K. Strategy for Stabilization of CutA1 Proteins Due to Ion-Ion Interactions at Temperatures of over 100 °C. Biochemistry. PMID 29648806 DOI: 10.1021/Acs.Biochem.8B00103 |
0.416 |
|
| 2017 |
Papini CM, Pandharipande PP, Royer CA, Makhatadze GI. Putting the Piezolyte Hypothesis under Pressure. Biophysical Journal. PMID 28803626 DOI: 10.1016/J.Bpj.2017.07.012 |
0.44 |
|
| 2017 |
Chen CR, Makhatadze GI. Molecular Determinants of Temperature Dependence of Protein Volume Change upon Unfolding. The Journal of Physical Chemistry. B. PMID 28795561 DOI: 10.1021/Acs.Jpcb.7B05831 |
0.462 |
|
| 2017 |
Walker KT, Nan R, Wright DW, Gor J, Bishop AC, Makhatadze GI, Brodsky B, Perkins SJ. Non-linearity of the collagen triple helix in solution and implications for collagen function. The Biochemical Journal. PMID 28533266 DOI: 10.1042/Bcj20170217 |
0.336 |
|
| 2017 |
Tzul FO, Vasilchuk D, Makhatadze GI. Reply to Candel et al.: Evidence for evolutionary conservation of folding kinetics in the thioredoxin protein family. Proceedings of the National Academy of Sciences of the United States of America. PMID 28512227 DOI: 10.1073/Pnas.1704669114 |
0.362 |
|
| 2017 |
Tzul FO, Vasilchuk D, Makhatadze GI. Evidence for the principle of minimal frustration in the evolution of protein folding landscapes. Proceedings of the National Academy of Sciences of the United States of America. PMID 28196883 DOI: 10.1073/Pnas.1613892114 |
0.498 |
|
| 2017 |
Chen CR, Makhatadze GI. Molecular determinant of the effects of hydrostatic pressure on protein folding stability. Nature Communications. 8: 14561. PMID 28169271 DOI: 10.1038/Ncomms14561 |
0.481 |
|
| 2017 |
Makhatadze GI. Linking computation and experiments to study the role of charge-charge interactions in protein folding and stability. Physical Biology. 14: 013002. PMID 28169222 DOI: 10.1088/1478-3975/14/1/013002 |
0.524 |
|
| 2016 |
Srivastava KR, French KC, Tzul FO, Makhatadze GI, Lapidus LJ. Intramolecular diffusion controls aggregation of the PAPf39 peptide. Biophysical Chemistry. 216: 37-43. PMID 27393931 DOI: 10.1016/J.Bpc.2016.06.004 |
0.302 |
|
| 2016 |
Shirke AN, Basore D, Holton S, Su A, Baugh E, Butterfoss GL, Makhatadze G, Bystroff C, Gross RA. Influence of surface charge, binding site residues and glycosylation on Thielavia terrestris cutinase biochemical characteristics. Applied Microbiology and Biotechnology. PMID 26758295 DOI: 10.1007/S00253-015-7254-1 |
0.423 |
|
| 2015 |
Tripathi S, Garcìa AE, Makhatadze GI. Alterations of Nonconserved Residues Affect Protein Stability and Folding Dynamics through Charge-Charge Interactions. The Journal of Physical Chemistry. B. 119: 13103-12. PMID 26413861 DOI: 10.1021/Acs.Jpcb.5B08527 |
0.509 |
|
| 2015 |
Pandharipande PP, Makhatadze GI. Applications of pressure perturbation calorimetry to study factors contributing to the volume changes upon protein unfolding. Biochimica Et Biophysica Acta. PMID 26341789 DOI: 10.1016/J.Bbagen.2015.08.021 |
0.347 |
|
| 2015 |
Chen CR, Makhatadze GI. ProteinVolume: calculating molecular van der Waals and void volumes in proteins. Bmc Bioinformatics. 16: 101. PMID 25885484 DOI: 10.1186/S12859-015-0531-2 |
0.456 |
|
| 2015 |
Pandharipande PP, Makhatadze GI. Thermal expansivities of peptides, polypeptides and proteins as measured by pressure perturbation calorimetry. Methods (San Diego, Calif.). 76: 61-6. PMID 25602591 DOI: 10.1016/J.Ymeth.2015.01.004 |
0.417 |
|
| 2015 |
Tzul FO, Schweiker KL, Makhatadze GI. Modulation of folding energy landscape by charge-charge interactions: linking experiments with computational modeling. Proceedings of the National Academy of Sciences of the United States of America. 112: E259-66. PMID 25564663 DOI: 10.1073/Pnas.1410424112 |
0.834 |
|
| 2015 |
Vargas-Uribe M, Rodnin MV, Öjemalm K, Holgado A, Kyrychenko A, Nilsson I, Posokhov YO, Makhatadze G, von Heijne G, Ladokhin AS. Thermodynamics of Membrane Insertion and Refolding of the Diphtheria Toxin T-Domain. The Journal of Membrane Biology. 248: 383-94. PMID 25281329 DOI: 10.1007/S00232-014-9734-0 |
0.312 |
|
| 2015 |
Tzul FO, Schweiker KL, Makhatadze GI. Modulation of folding energy landscape by charge-charge interactions:Linking experiments with computational modeling Proceedings of the National Academy of Sciences of the United States of America. 112: E259-E266. DOI: 10.1073/pnas.1410424112/-/DCSupplemental |
0.835 |
|
| 2014 |
Wafer LN, Tzul FO, Pandharipande PP, McCallum SA, Makhatadze GI. Structural and thermodynamic characterization of the recognition of the S100-binding peptides TRTK12 and p53 by calmodulin. Protein Science : a Publication of the Protein Society. 23: 1247-61. PMID 24947426 DOI: 10.1002/Pro.2506 |
0.375 |
|
| 2014 |
Vasilchuk D, Pandharipande PP, Suladze S, Sanchez-Ruiz JM, Makhatadze GI. Molecular determinants of expansivity of native globular proteins: a pressure perturbation calorimetry study. The Journal of Physical Chemistry. B. 118: 6117-22. PMID 24849138 DOI: 10.1021/Jp5028838 |
0.394 |
|
| 2014 |
French KC, Roan NR, Makhatadze GI. Structural characterization of semen coagulum-derived SEM1(86-107) amyloid fibrils that enhance HIV-1 infection. Biochemistry. 53: 3267-77. PMID 24811874 DOI: 10.1021/Bi500427R |
0.343 |
|
| 2014 |
Makhatadze G. Volume Changes Upon Unfolding of Globular Proteins: Computational and Experimental Studies Biophysical Journal. 106: 259a. DOI: 10.1016/J.Bpj.2013.11.1520 |
0.47 |
|
| 2013 |
Keshwani N, Banerjee S, Brodsky B, Makhatadze GI. The role of cross-chain ionic interactions for the stability of collagen model peptides. Biophysical Journal. 105: 1681-8. PMID 24094409 DOI: 10.1016/J.Bpj.2013.08.018 |
0.376 |
|
| 2013 |
Wafer LN, Tzul FO, Pandharipande PP, Makhatadze GI. Novel interactions of the TRTK12 peptide with S100 protein family members: specificity and thermodynamic characterization. Biochemistry. 52: 5844-56. PMID 23899389 DOI: 10.1021/Bi400788S |
0.387 |
|
| 2013 |
Tripathi S, Makhatadze GI, Garcia AE. Backtracking due to residual structure in the unfolded state changes the folding of the third fibronectin type III domain from tenascin-C. The Journal of Physical Chemistry. B. 117: 800-10. PMID 23268597 DOI: 10.1021/Jp310046K |
0.43 |
|
| 2013 |
Makhatadze G, Tzul F, Schweiker K. Effect of Ionizable Residues on the Folding Energy Landscape of Globular Proteins: Linking Experiment and Computation Biophysical Journal. 104: 189a. DOI: 10.1016/J.Bpj.2012.11.1067 |
0.833 |
|
| 2013 |
Canchi DR, Jayasimha P, Rao DC, Makhatadze GI, Garcia AE. Molecular Mechanism for the Preferential Exclusion of Osmolytes from Protein Surfaces Biophysical Journal. 104: 189a. DOI: 10.1016/J.Bpj.2012.11.1065 |
0.506 |
|
| 2012 |
Canchi DR, Jayasimha P, Rau DC, Makhatadze GI, Garcia AE. Molecular mechanism for the preferential exclusion of TMAO from protein surfaces. The Journal of Physical Chemistry. B. 116: 12095-104. PMID 22970901 DOI: 10.1021/Jp304298C |
0.528 |
|
| 2012 |
Wafer LN, Streicher WW, McCallum SA, Makhatadze GI. Thermodynamic and kinetic analysis of peptides derived from CapZ, NDR, p53, HDM2, and HDM4 binding to human S100B. Biochemistry. 51: 7189-201. PMID 22913742 DOI: 10.1021/Bi300865G |
0.356 |
|
| 2012 |
Scian M, Lin JC, Le Trong I, Makhatadze GI, Stenkamp RE, Andersen NH. Crystal and NMR structures of a Trp-cage mini-protein benchmark for computational fold prediction. Proceedings of the National Academy of Sciences of the United States of America. 109: 12521-5. PMID 22802678 DOI: 10.1073/Pnas.1121421109 |
0.382 |
|
| 2012 |
Chan CH, Wilbanks CC, Makhatadze GI, Wong KB. Electrostatic contribution of surface charge residues to the stability of a thermophilic protein: benchmarking experimental and predicted pKa values. Plos One. 7: e30296. PMID 22279578 DOI: 10.1371/Journal.Pone.0030296 |
0.555 |
|
| 2012 |
Zarrine-Afsar A, Zhang Z, Schweiker KL, Makhatadze GI, Davidson AR, Chan HS. Kinetic consequences of native state optimization of surface-exposed electrostatic interactions in the Fyn SH3 domain. Proteins. 80: 858-70. PMID 22161863 DOI: 10.1002/Prot.23243 |
0.825 |
|
| 2012 |
Jayasimha P, Shanmuganathan A, Suladze S, Makhatadze GI. Contribution of buried aspartic acid to the stability of the PDZ2 protein Journal of Chemical Thermodynamics. 52: 64-68. DOI: 10.1016/J.Jct.2012.01.021 |
0.509 |
|
| 2011 |
Loladze VV, Makhatadze GI. Energetics of charge-charge interactions between residues adjacent in sequence. Proteins. 79: 3494-9. PMID 22072523 DOI: 10.1002/Prot.23132 |
0.817 |
|
| 2011 |
Jimenez-Cruz CA, Makhatadze GI, Garcia AE. Protonation/deprotonation effects on the stability of the Trp-cage miniprotein. Physical Chemistry Chemical Physics : Pccp. 13: 17056-63. PMID 21773639 DOI: 10.1039/C1Cp21193E |
0.475 |
|
| 2011 |
Patel MM, Tzul F, Makhatadze GI. Equilibrium and kinetic studies of protein cooperativity using urea-induced folding/unfolding of a Ubq-UIM fusion protein. Biophysical Chemistry. 159: 58-65. PMID 21621903 DOI: 10.1016/J.Bpc.2011.05.004 |
0.473 |
|
| 2011 |
Bush J, Makhatadze GI. Statistical analysis of protein structures suggests that buried ionizable residues in proteins are hydrogen bonded or form salt bridges. Proteins. 79: 2027-32. PMID 21560169 DOI: 10.1002/Prot.23067 |
0.489 |
|
| 2010 |
Patel MM, Sgourakis NG, Garcia AE, Makhatadze GI. Experimental test of the thermodynamic model of protein cooperativity using temperature-induced unfolding of a Ubq-UIM fusion protein. Biochemistry. 49: 8455-67. PMID 20836541 DOI: 10.1021/Bi101163U |
0.488 |
|
| 2010 |
Tsamaloukas AD, Pyzocha NK, Makhatadze GI. Pressure perturbation calorimetry of unfolded proteins. The Journal of Physical Chemistry. B. 114: 16166-70. PMID 20831285 DOI: 10.1021/Jp106294P |
0.346 |
|
| 2010 |
Streicher WW, Lopez MM, Makhatadze GI. Modulation of quaternary structure of S100 proteins by calcium ions. Biophysical Chemistry. 151: 181-6. PMID 20621410 DOI: 10.1016/J.Bpc.2010.06.003 |
0.42 |
|
| 2010 |
Wafer LN, Streicher WW, Makhatadze GI. Thermodynamics of the Trp-cage miniprotein unfolding in urea. Proteins. 78: 1376-81. PMID 20112418 DOI: 10.1002/Prot.22681 |
0.416 |
|
| 2010 |
Sgourakis NG, Patel MM, Garcia AE, Makhatadze GI, McCallum SA. Conformational dynamics and structural plasticity play critical roles in the ubiquitin recognition of a UIM domain. Journal of Molecular Biology. 396: 1128-44. PMID 20053359 DOI: 10.1016/J.Jmb.2009.12.052 |
0.473 |
|
| 2010 |
Chung WK, Hou Y, Holstein M, Freed A, Makhatadze GI, Cramer SM. Investigation of protein binding affinity in multimodal chromatographic systems using a homologous protein library. Journal of Chromatography. A. 1217: 191-8. PMID 19732898 DOI: 10.1016/J.Chroma.2009.08.005 |
0.511 |
|
| 2009 |
Schweiker KL, Makhatadze GI. Use of pressure perturbation calorimetry to characterize the volumetric properties of proteins. Methods in Enzymology. 466: 527-47. PMID 21609875 DOI: 10.1016/S0076-6879(09)66022-5 |
0.79 |
|
| 2009 |
Schweiker KL, Fitz VW, Makhatadze GI. Universal convergence of the specific volume changes of globular proteins upon unfolding. Biochemistry. 48: 10846-51. PMID 19877593 DOI: 10.1016/J.Bpj.2009.12.3353 |
0.828 |
|
| 2009 |
Streicher WW, Lopez MM, Makhatadze GI. Annexin I and annexin II N-terminal peptides binding to S100 protein family members: specificity and thermodynamic characterization. Biochemistry. 48: 2788-98. PMID 19275165 DOI: 10.1021/Bi8019959 |
0.391 |
|
| 2009 |
Schweiker KL, Makhatadze GI. A computational approach for the rational design of stable proteins and enzymes: optimization of surface charge-charge interactions. Methods in Enzymology. 454: 175-211. PMID 19216927 DOI: 10.1016/S0076-6879(08)03807-X |
0.83 |
|
| 2009 |
Gribenko AV, Patel MM, Liu J, McCallum SA, Wang C, Makhatadze GI. Rational stabilization of enzymes by computational redesign of surface charge-charge interactions. Proceedings of the National Academy of Sciences of the United States of America. 106: 2601-6. PMID 19196981 DOI: 10.1073/Pnas.0808220106 |
0.777 |
|
| 2009 |
Schweiker KL, Makhatadze GI. Protein stabilization by the rational design of surface charge-charge interactions. Methods in Molecular Biology (Clifton, N.J.). 490: 261-83. PMID 19157087 DOI: 10.1007/978-1-59745-367-7_11 |
0.829 |
|
| 2009 |
Chung WK, Hou Y, Freed A, Holstein M, Makhatadze GI, Cramer SM. Investigation of protein binding affinity and preferred orientations in ion exchange systems using a homologous protein library. Biotechnology and Bioengineering. 102: 869-81. PMID 18821632 DOI: 10.1002/Bit.22100 |
0.529 |
|
| 2008 |
Bale S, Lopez MM, Makhatadze GI, Fang Q, Pegg AE, Ealick SE. Structural basis for putrescine activation of human S-adenosylmethionine decarboxylase. Biochemistry. 47: 13404-17. PMID 19053272 DOI: 10.1021/Bi801732M |
0.346 |
|
| 2008 |
Gvritishvili AG, Gribenko AV, Makhatadze GI. Cooperativity of complex salt bridges. Protein Science : a Publication of the Protein Society. 17: 1285-90. PMID 18469176 DOI: 10.1110/Ps.034975.108 |
0.705 |
|
| 2008 |
Makhatadze GI. Thermal Unfolding of Proteins Studied by Calorimetry Protein Folding Handbook. 1: 70-98. DOI: 10.1002/9783527619498.ch4 |
0.307 |
|
| 2007 |
Schweiker KL, Zarrine-Afsar A, Davidson AR, Makhatadze GI. Computational design of the Fyn SH3 domain with increased stability through optimization of surface charge charge interactions. Protein Science : a Publication of the Protein Society. 16: 2694-702. PMID 18029422 DOI: 10.1110/Ps.073091607 |
0.84 |
|
| 2007 |
Streicher WW, Makhatadze GI. Unfolding thermodynamics of Trp-cage, a 20 residue miniprotein, studied by differential scanning calorimetry and circular dichroism spectroscopy. Biochemistry. 46: 2876-80. PMID 17295518 DOI: 10.1021/Bi602424X |
0.442 |
|
| 2007 |
Gribenko AV, Makhatadze GI. Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins. Journal of Molecular Biology. 366: 842-56. PMID 17188709 DOI: 10.1016/J.Jmb.2006.11.061 |
0.804 |
|
| 2007 |
Streicher WW, Makhatadze GI. Advances in the analysis of conformational transitions in peptides using differential scanning calorimetry. Methods in Molecular Biology (Clifton, N.J.). 350: 105-13. PMID 16957320 DOI: 10.1385/1-59745-189-4:105 |
0.353 |
|
| 2007 |
Ermolenko DN, Dangi B, Gvritishvili A, Gronenborn AM, Makhatadze GI. Elimination of the C-cap in ubiquitin-structure, dynamics and thermodynamic consequences Biophysical Chemistry. 126: 25-35. PMID 16713063 DOI: 10.1016/J.Bpc.2006.03.017 |
0.477 |
|
| 2006 |
Gribenko AV, Keiffer TR, Makhatadze GI. Amino acid substitutions affecting protein dynamics in eglin C do not affect heat capacity change upon unfolding. Proteins. 64: 295-300. PMID 16705642 DOI: 10.1002/Prot.20974 |
0.74 |
|
| 2006 |
Strickler SS, Gribenko AV, Gribenko AV, Keiffer TR, Tomlinson J, Reihle T, Loladze VV, Makhatadze GI. Protein stability and surface electrostatics: a charged relationship. Biochemistry. 45: 2761-6. PMID 16503630 DOI: 10.1021/Bi0600143 |
0.837 |
|
| 2006 |
Bang D, Gribenko AV, Tereshko V, Kossiakoff AA, Kent SB, Makhatadze GI. Dissecting the energetics of protein alpha-helix C-cap termination through chemical protein synthesis. Nature Chemical Biology. 2: 139-43. PMID 16446709 DOI: 10.1038/Nchembio766 |
0.737 |
|
| 2006 |
Streicher WW, Makhatadze GI. Calorimetric evidence for a two-state unfolding of the beta-hairpin peptide trpzip4. Journal of the American Chemical Society. 128: 30-1. PMID 16390106 DOI: 10.1021/Ja056392X |
0.34 |
|
| 2005 |
Makhatadze GI. Thermodynamics Of alpha-Helix Formation. Advances in Protein Chemistry. 72: 199-226. PMID 16581378 DOI: 10.1016/S0065-3233(05)72008-8 |
0.357 |
|
| 2005 |
Lee CF, Makhatadze GI, Wong KB. Effects of charge-to-alanine substitutions on the stability of ribosomal protein L30e from Thermococcus celer. Biochemistry. 44: 16817-25. PMID 16363795 DOI: 10.1021/Bi0519654 |
0.56 |
|
| 2005 |
Permyakov SE, Makhatadze GI, Owenius R, Uversky VN, Brooks CL, Permyakov EA, Berliner LJ. How to improve nature: study of the electrostatic properties of the surface of alpha-lactalbumin. Protein Engineering, Design & Selection : Peds. 18: 425-33. PMID 16093284 DOI: 10.1093/Protein/Gzi051 |
0.381 |
|
| 2005 |
Bang D, Makhatadze GI, Tereshko V, Kossiakoff AA, Kent SB. Total chemical synthesis and X-ray crystal structure of a protein diastereomer: [D-Gln 35]ubiquitin. Angewandte Chemie (International Ed. in English). 44: 3852-6. PMID 15834850 DOI: 10.1002/Anie.200463040 |
0.361 |
|
| 2005 |
Richardson JM, Lopez MM, Makhatadze GI. Enthalpy of helix-coil transition: missing link in rationalizing the thermodynamics of helix-forming propensities of the amino acid residues. Proceedings of the National Academy of Sciences of the United States of America. 102: 1413-8. PMID 15671166 DOI: 10.1073/Pnas.0408004102 |
0.396 |
|
| 2005 |
Loladze VV, Makhatadze GI. Both helical propensity and side-chain hydrophobicity at a partially exposed site in alpha-helix contribute to the thermodynamic stability of ubiquitin. Proteins. 58: 1-6. PMID 15515183 DOI: 10.1002/Prot.20283 |
0.815 |
|
| 2004 |
Lee YC, Volk DE, Thiviyanathan V, Kleerekoper Q, Gribenko AV, Zhang S, Gorenstein DG, Makhatadze GI, Luxon BA. Letter to the editor: NMR structure of the apo-S100P protein [4] Journal of Biomolecular Nmr. 29: 399-402. PMID 15213440 DOI: 10.1023/B:Jnmr.0000032617.88899.4B |
0.698 |
|
| 2004 |
Makhatadze GI, Loladze VV, Gribenko AV, Lopez MM. Mechanism of thermostabilization in a designed cold shock protein with optimized surface electrostatic interactions. Journal of Molecular Biology. 336: 929-42. PMID 15095870 DOI: 10.1016/J.Jmb.2003.12.058 |
0.822 |
|
| 2004 |
Richardson JM, Makhatadze GI. Temperature dependence of the thermodynamics of helix-coil transition. Journal of Molecular Biology. 335: 1029-37. PMID 14698297 DOI: 10.1016/J.Jmb.2003.11.027 |
0.34 |
|
| 2003 |
Ermolenko DN, Richardson JM, Makhatadze GI. Noncharged amino acid residues at the solvent-exposed positions in the middle and at the C terminus of the alpha-helix have the same helical propensity. Protein Science : a Publication of the Protein Society. 12: 1169-76. PMID 12761387 DOI: 10.1110/Ps.0304303 |
0.439 |
|
| 2003 |
Makhatadze GI, Loladze VV, Ermolenko DN, Chen X, Thomas ST. Contribution of surface salt bridges to protein stability: guidelines for protein engineering. Journal of Molecular Biology. 327: 1135-48. PMID 12662936 DOI: 10.1016/S0022-2836(03)00233-X |
0.821 |
|
| 2002 |
Ermolenko DN, Makhatadze GI. Bacterial cold-shock proteins Cellular and Molecular Life Sciences. 59: 1902-1913. PMID 12530521 DOI: 10.1007/Pl00012513 |
0.342 |
|
| 2002 |
Ermolenko DN, Thomas ST, Aurora R, Gronenborn AM, Makhatadze GI. Hydrophobic interactions at the Ccap position of the C-capping motif of alpha-helices. Journal of Molecular Biology. 322: 123-35. PMID 12215419 DOI: 10.1016/S0022-2836(02)00734-9 |
0.455 |
|
| 2002 |
Loladze VV, Ermolenko DN, Makhatadze GI. Thermodynamic consequences of burial of polar and non-polar amino acid residues in the protein interior. Journal of Molecular Biology. 320: 343-57. PMID 12079391 DOI: 10.1016/S0022-2836(02)00465-5 |
0.798 |
|
| 2002 |
Gribenko AV, Guzmán-Casado M, Lopez MM, Makhatadze GI. Conformational and thermodynamic properties of peptide binding to the human S100P protein. Protein Science : a Publication of the Protein Society. 11: 1367-75. PMID 12021435 DOI: 10.1110/Ps.0202202 |
0.705 |
|
| 2002 |
Lopez MM, Chin DH, Baldwin RL, Makhatadze GI. The enthalpy of the alanine peptide helix measured by isothermal titration calorimetry using metal-binding to induce helix formation. Proceedings of the National Academy of Sciences of the United States of America. 99: 1298-302. PMID 11818561 DOI: 10.1073/Pnas.032665199 |
0.349 |
|
| 2002 |
Loladze VV, Makhatadze GI. Removal of surface charge-charge interactions from ubiquitin leaves the protein folded and very stable. Protein Science : a Publication of the Protein Society. 11: 174-7. PMID 11742133 DOI: 10.1110/Ps.29902 |
0.843 |
|
| 2001 |
Makhatadze GI. Measuring protein thermostability by differential scanning calorimetry Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. PMID 18429202 DOI: 10.1002/0471140864.Ps0709S12 |
0.386 |
|
| 2001 |
Gribenko AV, Hopper JE, Makhatadze GI. Molecular characterization and tissue distribution of a novel member of the S100 family of EF-hand proteins. Biochemistry. 40: 15538-48. PMID 11747429 DOI: 10.1021/Bi0114731 |
0.732 |
|
| 2001 |
Thomas ST, Loladze VV, Makhatadze GI. Hydration of the peptide backbone largely defines the thermodynamic propensity scale of residues at the C' position of the C-capping box of alpha-helices. Proceedings of the National Academy of Sciences of the United States of America. 98: 10670-5. PMID 11535835 DOI: 10.1073/Pnas.191381798 |
0.792 |
|
| 2001 |
Loladze VV, Ermolenko DN, Makhatadze GI. Heat capacity changes upon burial of polar and nonpolar groups in proteins. Protein Science : a Publication of the Protein Society. 10: 1343-52. PMID 11420436 DOI: 10.1110/Ps.370101 |
0.787 |
|
| 2001 |
Lopez MM, Yutani K, Makhatadze GI. Interactions of the cold shock protein CspB from bacillus subtilis with single-stranded DNA. Importance of the T base content and position within the template Journal of Biological Chemistry. 276: 15511-15518. PMID 11278683 DOI: 10.1074/Jbc.M010474200 |
0.321 |
|
| 2001 |
Sanchez-Ruiz JM, Makhatadze GI. To charge or not to charge? Trends in Biotechnology. 19: 132-135. PMID 11250029 DOI: 10.1016/S0167-7799(00)01548-1 |
0.526 |
|
| 2000 |
Richardson JM, Lemaire SD, Jacquot JP, Makhatadze GI. Difference in the mechanisms of the cold and heat induced unfolding of thioredoxin h from Chlamydomonas reinhardtii: spectroscopic and calorimetric studies. Biochemistry. 39: 11154-62. PMID 10998255 DOI: 10.1021/Bi000610B |
0.372 |
|
| 2000 |
Thomas ST, Makhatadze GI. Contribution of the 30/36 hydrophobic contact at the C-terminus of the alpha-helix to the stability of the ubiquitin molecule. Biochemistry. 39: 10275-83. PMID 10956017 DOI: 10.1021/Bi0000418 |
0.429 |
|
| 2000 |
Lopez MM, Makhatadze GI. Major cold shock proteins, CspA from Escherichia coli and CspB from Bacillus subtilis, interact differently with single-stranded DNA templates Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1479: 196-202. PMID 10862969 DOI: 10.1016/S0167-4838(00)00048-0 |
0.408 |
|
| 2000 |
Petrosian SA, Makhatadze GI. Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA. Protein Science : a Publication of the Protein Society. 9: 387-94. PMID 10716191 DOI: 10.1110/Ps.9.2.387 |
0.525 |
|
| 2000 |
Lemaire SD, Richardson JM, Goyer A, Keryer E, Lancelin JM, Makhatadze GI, Jacquot JP. Primary structure determinants of the pH- and temperature-dependent aggregation of thioredoxin. Biochimica Et Biophysica Acta. 1476: 311-23. PMID 10669795 DOI: 10.1016/S0167-4838(99)00235-6 |
0.328 |
|
| 1999 |
Loladze VV, Ibarra-Molero B, Sanchez-Ruiz JM, Makhatadze GI. Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface. Biochemistry. 38: 16419-23. PMID 10600102 DOI: 10.1021/Bi992271W |
0.833 |
|
| 1999 |
Lopez MM, Yutani K, Makhatadze GI. Interactions of the major cold shock protein of Bacillus subtilis CspB with single-stranded DNA templates of different base composition Journal of Biological Chemistry. 274: 33601-33608. PMID 10559248 DOI: 10.1074/Jbc.274.47.33601 |
0.403 |
|
| 1999 |
Pace CN, Grimsley GR, Thomas ST, Makhatadze GI. Heat capacity change for ribonuclease A folding. Protein Science : a Publication of the Protein Society. 8: 1500-4. PMID 10422839 DOI: 10.1110/Ps.8.7.1500 |
0.348 |
|
| 1999 |
Ibarra-Molero B, Loladze VV, Makhatadze GI, Sanchez-Ruiz JM. Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability. Biochemistry. 38: 8138-49. PMID 10387059 DOI: 10.1021/Bi9905819 |
0.827 |
|
| 1999 |
Ibarra-Molero B, Makhatadze GI, Sanchez-Ruiz JM. Cold denaturation of ubiquitin Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1429: 384-390. PMID 9989223 DOI: 10.1016/S0167-4838(98)00252-0 |
0.347 |
|
| 1999 |
Makhatadze GI. Thermodynamics of protein interactions with urea and guanidinium hydrochloride Journal of Physical Chemistry B. 103: 4784-4785. DOI: 10.1021/Jp990413Q |
0.478 |
|
| 1998 |
Lopez MM, Makhatadze GI. Solvent isotope effect on thermodynamics of hydration. Biophysical Chemistry. 74: 117-25. PMID 17029738 DOI: 10.1016/S0301-4622(98)00173-2 |
0.303 |
|
| 1998 |
Gribenko AV, Makhatadze GI. Oligomerization and divalent ion binding properties of the S100P protein: a Ca2+/Mg2+-switch model. Journal of Molecular Biology. 283: 679-94. PMID 9784376 DOI: 10.1006/Jmbi.1998.2116 |
0.688 |
|
| 1998 |
Makhatadze GI. Heat capacities of amino acids, peptides and proteins Biophysical Chemistry. 71: 133-156. PMID 9648205 DOI: 10.1016/S0301-4622(98)00095-7 |
0.405 |
|
| 1998 |
Makhatadze GI, Lopez MM, Richardson JM, Thomas ST. Anion binding to the ubiquitin molecule. Protein Science : a Publication of the Protein Society. 7: 689-97. PMID 9541401 DOI: 10.1002/Pro.5560070318 |
0.35 |
|
| 1998 |
Gribenko A, Lopez MM, Richardson JM, Makhatadze GI. Cloning, overexpression, purification, and spectroscopic characterization of human S100P. Protein Science : a Publication of the Protein Society. 7: 211-5. PMID 9514277 DOI: 10.1002/Pro.5560070123 |
0.694 |
|
| 1997 |
Makhatadze GI, Lopez MM, Privalov PL. Heat capacities of protein functional groups Biophysical Chemistry. 64: 93-101. DOI: 10.1016/S0301-4622(96)02234-X |
0.6 |
|
| 1996 |
Makhatadze GI, Privalov PL. On the entropy of protein folding Protein Science. 5: 507-510. PMID 8868487 DOI: 10.1002/Pro.5560050312 |
0.68 |
|
| 1995 |
Makhatadze GI, Privalov PL. Energetics of protein structure Advances in Protein Chemistry. 47: 307-425. PMID 8561051 DOI: 10.1016/S0065-3233(08)60548-3 |
0.7 |
|
| 1995 |
Makhatadze GI, Clore GM, Gronenborn AM. Solvent isotope effect and protein stability Nature Structural Biology. 2: 852-855. PMID 7552708 DOI: 10.1038/Nsb1095-852 |
0.509 |
|
| 1994 |
Wintrode PL, Makhatadze GI, Privalov PL. Thermodynamics of ubiquitin unfolding Proteins: Structure, Function and Genetics. 18: 246-253. PMID 8202465 DOI: 10.1002/Prot.340180305 |
0.65 |
|
| 1994 |
Yu Y, Makhatadze GI, Pace CN, Privalov PL. Energetics of ribonuclease T1 structure Biochemistry. 33: 3312-3319. PMID 8136367 DOI: 10.1021/Bi00177A023 |
0.648 |
|
| 1994 |
Makhatadze GI, Clore GM, Gronenborn AM, Privalov PL. Thermodynamics of unfolding of the all β-sheet protein interleukin-1β Biochemistry. 33: 9327-9332. PMID 8049234 DOI: 10.1021/bi00197a037 |
0.572 |
|
| 1994 |
Makhatadze GI, Privalov PL. Energetics of interactions of aromatic hydrocarbons with water Biophysical Chemistry. 50: 285-291. PMID 8011949 DOI: 10.1016/0301-4622(93)E0096-N |
0.591 |
|
| 1994 |
Griko YV, Makhatadze GI, Privalov PL, Hartley RW. Thermodynamics of barnase unfolding Protein Science. 3: 669-676. PMID 8003984 DOI: 10.1002/Pro.5560030414 |
0.67 |
|
| 1994 |
Makhatadze GI, Privalov PL. Hydration effects in protein unfolding Biophysical Chemistry. 51: 291-309. PMID 7919040 DOI: 10.1016/0301-4622(94)00050-6 |
0.706 |
|
| 1994 |
Makhatadze GI, Marahiel MA. Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis Protein Science. 3: 2144-2147. PMID 7703860 DOI: 10.1002/Pro.5560031127 |
0.407 |
|
| 1993 |
Privalov PL, Makhatadze GI. Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration Journal of Molecular Biology. 232: 660-679. PMID 8393941 DOI: 10.1006/Jmbi.1993.1417 |
0.663 |
|
| 1993 |
Makhatadze GI, Privalov PL. Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration Journal of Molecular Biology. 232: 639-659. PMID 8393940 DOI: 10.1006/Jmbi.1993.1416 |
0.66 |
|
| 1993 |
Makhatadze GI, Kim KS, Woodward C, Privalov PL. Thermodynamics of BPTI folding Protein Science. 2: 2028-2036. PMID 7507751 DOI: 10.1002/Pro.5560021204 |
0.627 |
|
| 1993 |
Makhatadze GI, Fernandez J, Freire E, Lilley TH, Privalov PL. Thermodynamics of aqueous guanidinium hydrochloride solutions in the temperature range from 283.15 to 313.15 K Journal of Chemical & Engineering Data. 38: 83-87. DOI: 10.1021/Je00009A020 |
0.562 |
|
| 1992 |
Makhatadze GI, Privalov PL. Protein interactions with urea and guanidinium chloride. A calorimetric study Journal of Molecular Biology. 226: 491-505. PMID 1322462 DOI: 10.1016/0022-2836(92)90963-K |
0.659 |
|
| 1992 |
Privalov PL, Makhatadze GI. Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfolding Journal of Molecular Biology. 224: 715-723. PMID 1314903 DOI: 10.1016/0022-2836(92)90555-X |
0.653 |
|
| 1990 |
Makhatadze GI, Gill SJ, Privalov PL. Partial molar heat capacities of the side chains of some amino acid residues in aqueous solution. The influence of the neighboring charges. Biophysical Chemistry. 38: 33-7. PMID 17056435 DOI: 10.1016/0301-4622(90)80037-8 |
0.578 |
|
| 1990 |
Makhatadze GI, Privalov PL. Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: Hydration effect Journal of Molecular Biology. 213: 375-384. PMID 2342113 DOI: 10.1016/S0022-2836(05)80197-4 |
0.623 |
|
| 1990 |
Privalov PL, Makhatadze GI. Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: Protein unfolding effects Journal of Molecular Biology. 213: 385-391. PMID 2160545 DOI: 10.1016/S0022-2836(05)80198-6 |
0.651 |
|
| 1990 |
Makhatadze GI, Medvedkin VN, Privalov PL. Partial molar volumes of polypeptides and their constituent groups in aqueous solution over a broad temperature range Biopolymers. 30: 1001-1010. PMID 2081262 DOI: 10.1002/Bip.360301102 |
0.632 |
|
| 1989 |
Privalov PL, Tiktopulo EI, Venyaminov SY, Griko YV, Makhatadze GI, Khechinashvili NN. Heat capacity and conformation of proteins in the denatured state Journal of Molecular Biology. 205: 737-750. PMID 2538636 DOI: 10.1016/0022-2836(89)90318-5 |
0.629 |
|
| 1989 |
Makhatadze GI, Privalov PL. Heat capacity of alcohols in aqueous solutions in the temperature range from 5 to 125°C Journal of Solution Chemistry. 18: 927-936. DOI: 10.1007/BF00647893 |
0.532 |
|
| 1988 |
Makhatadze GI, Privalov PL. Partial specific heat capacity of benzene and of toluene in aqueous solution determined calorimetrically for a broad temperature range The Journal of Chemical Thermodynamics. 20: 405-412. DOI: 10.1016/0021-9614(88)90177-2 |
0.539 |
|
| Show low-probability matches. |
